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2016 Nov 03;51:1998. doi: 10.1186/s40064-016-3484-7.
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Characterization of a novel hatching enzyme purified from starfish Asterina pectinifera.
Choi JH
,
Kim SM
.
???displayArticle.abstract??? Hatching enzyme is a protease which can degrade the membrane of egg. In this study, a hatching enzyme was purified from starfish (Asterina pectinifera) with 6.34 fold of purification rate, 5.04 % of yield, and 73.87 U/mg of specific activity. The molecular weight of starfish hatching enzyme was 86 kDa, which was reduced to 62 kDa after removal of N-linked oligosaccharides. The optimal pH and temperature of the hatching enzyme activity were pH 7.0 and 40 °C, respectively, while those of stability were pH 8 and 20 °C. The kinetic parameters, V
max
, K
m
, K
cat
and K
cat
/K
m
values were 0.197 U/ml, 0.289 mg/ml, 112.57 s-1, and 389.52 ml/mg s, respectively. Zn2+ increased the enzyme activity by 167.28 %, while EDTA, TPCK, TGCK, leupeptin, PMSF, and TLCK decreased. In addition, Ca2+, Mg2+, and Cu2+ did not affect the enzyme activity. The starfish hatching enzyme activity pretreated with EDTA was recovered by Zn2+. Therefore, the starfish hatching enzyme was classified as a serine-zinc protease.
Fig. 1. Elution profile of the starfish hatching enzyme. a DEAE-Ion exchange chromatography. b Sephachryl gel filtration chromatography
Fig. 2. SDS-PAGE pattern of the Starfish hatching enzyme. The acrylamide concentration of the separation gel was 12 % and protein bands were stained with Coomassie Brilliant Blue. A Purified hatching enzyme from Sephacryl gel filtration. B N-glycan deglycosylation of the purified hatching enzyme by treatment with PNGase F. Lane M standard molecular weight markers
Fig. 3. Effects of pH and temperature on the proteolytic activity and stability of hatching enzyme
Fig. 4. Recovery effect of metal ions on the EDTA pretreated starfish hatching enzyme
Fig. 5. Michaelis–Menten kinetic curve a and Lineweaver-Bulk plots b of the starfish hatching enzyme
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